Urea-Elicited Changes in Relative Electrophoretic Mobility of Certain Glycinin and β-Conglycinin Subunits

Abstract

Six molar urea in sodium dodecyl sulfate-polyacrylamide gels altered the relative electrophoretic mobility of several soybean protein subunits. Glycinin acidic polypeptide components A(3) and A(4) could be resolved from the other acidic polypeptides. A variant of the delta' subunit of beta-conglycinin was identified.